Proceedings of the National Academy of Sciences · 1981 · 686 citations · 27 references
Life SciencesBiochemistryCell BiologyClinical ImmunologyEndocytosisTumor MicroenvironmentAntibody PurificationCell CharacterizationCell Surface GlycoproteinsGlycoprotein AnalysisSurface Antigen IdentificationTumor-associated Glycoproteins
A cell surface glycoprotein antigen with an apparent molecular weight of about 100,000 that is selectively expressed on proliferating cells was purified from deoxycholate-solubilized membranes of a cultured human leukemic thymus-derived (T) cell line by affinity chromatography on a monoclonal antibody-Sepharose column. A conventional xenoantiserum prepared by immunization with the affinity-purified glycoprotein was found to contain antibodies against a serum component that bound tightly to cultured cells. This molecule was shown to be specifically associated with the cell surface glycoprotein purified by immunoprecipitation from lysates of cells. We have identified the serum component as transferrin and conclude that the membrane glycoprotein is the cell surface transferrin receptor.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
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Protein Purification by Affinity Chromatography
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Ellis L. Reinherz, Patrick C. Kung, Gideon Goldstein et al. · Proceedings of the National Academy of Sciences · 1980 · 1.6K citations · Full text
Life Sciences, Immunology, Oncology +17